ID   APS1_SCHPO              Reviewed;         210 AA.
AC   Q09790;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase aps1;
DE            EC=3.6.1.52;
DE   AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase;
DE            Short=Ap6A hydrolase;
DE            EC=3.6.1.-;
GN   Name=aps1; ORFNames=SPAC13G6.14, SPAC24B11.03;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=99192402; PubMed=10090752; DOI=10.1021/bi982951j;
RA   Ingram S.W., Stratemann S.A., Barnes L.D.;
RT   "Schizosaccharomyces pombe Aps1, a diadenosine 5',5'''-P1, P6-
RT   hexaphosphate hydrolase that is a member of the nudix (MutT) family of
RT   hydrolases: cloning of the gene and characterization of the purified
RT   enzyme.";
RL   Biochemistry 38:3649-3655(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=99348303; PubMed=10419486; DOI=10.1074/jbc.274.31.21735;
RA   Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G.,
RA   Barnes L.D., Shears S.B.;
RT   "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces
RT   pombe and Saccharomyces cerevisiae are homologues of the human
RT   diphosphoinositol polyphosphate phosphohydrolase. Overlapping
RT   substrate specificities in a MutT-type protein.";
RL   J. Biol. Chem. 274:21735-21740(1999).
RN   [4]
RP   ENZYME ACTIVITY, AND MUTAGENESIS OF GLU-93.
RX   PubMed=12387729; DOI=10.1042/BJ20020733;
RA   Ingram S.W., Safrany S.T., Barnes L.D.;
RT   "Disruption and overexpression of the Schizosaccharomyces pombe aps1
RT   gene, and effects on growth rate, morphology and intracellular
RT   diadenosine 5',5''-P1,P5-pentaphosphate and diphosphoinositol
RT   polyphosphate concentrations.";
RL   Biochem. J. 369:519-528(2003).
CC   -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in
CC       PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4
CC       (bisdiphosphoinositol tetrakisphosphate). Also catalyzes the
CC       hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A
CC       being the preferred substrates. The major reaction products are
CC       ADP and p4a from Ap6A and ADP and ATP from Ap5A.
CC   -!- CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H(2)O =
CC       myo-inositol polyphosphate + phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=31 nM for PP-InsP5;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
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DR   EMBL; AF125215; AAD20015.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA91107.1; -; Genomic_DNA.
DR   PIR; S62443; S62443.
DR   RefSeq; NP_592840.1; -.
DR   GeneID; 2542890; -.
DR   KEGG; spo:SPAC13G6.14; -.
DR   NMPDR; fig|4896.1.peg.2810; -.
DR   GeneDB_Spombe; SPAC13G6.14; -.
DR   OMA; Q09790; WMREALQ.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000511-MON; -.
DR   BRENDA; 3.6.1.52; 653.
DR   ArrayExpress; Q09790; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphata...; IDA:GeneDB_SPombe.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015959; P:diadenosine polyphosphate metabolic process; IDA:GeneDB_SPombe.
DR   InterPro; IPR000086; NUDIX_hydrolase_core.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    210       Diphosphoinositol polyphosphate
FT                                phosphohydrolase aps1.
FT                                /FTId=PRO_0000057068.
FT   MOTIF        74     95       Nudix box.
FT   METAL        89     89       Magnesium (By similarity).
FT   METAL        93     93       Magnesium (By similarity).
FT   MUTAGEN      93     93       E->Q: Does not affect intracellular Ap5A
FT                                level, but strongly reduces DIPP enzyme
FT                                activity.
SQ   SEQUENCE   210 AA;  23724 MW;  492F7BF9563A1C98 CRC64;
     MLENNGSVIL MEPDHLRTAV NRSMTSREGR TKNRFNPITG ARLAAGVVAL SADKRKVLLV
     SSAKKHPSWV VPKGGWEADE SVQQAALREG WEEGGLVGHI TRSLGSFKDK RPTDTIDRRK
     KYLKQLMSKS SGNDVSTNTE LGAEAEKLLL PPRAECEFFE VIVERLEDNY PEMRKRRRKW
     MSYQEAKEAL TSRKDILAAL EKSSIIKEEN
//